Abstract

Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts.

Key points

• The sequence similarity network of OYEs superfamily was constructed and annotated.

• The structures and active sites of OYEs from different classes were compared.

• “Left/right” binding mode was used to explain the stereopreferences of OYEs.

• Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed.

中文翻译：

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旧的黄色酶：立体互补生物还原的结构和结构指导工程。

摘要

自首次发现来自酵母菌的旧黄色酶1（OYE1）在1932年，通过OYE进行的生物催化不对称还原活化烯烃已成为有机合成中的重要反应。为了获得立体互补的C = C键生物还原，已经进行了新型OYE的挖掘，尤其是现有OYE的蛋白质工程，成功地在几种情况下实现了立体互补的还原，并进一步提高了应用潜力。在这篇综述中，我们分析了OYEs的结构，活性位点和底物识别，这是其底物特异性和立体特异性的基础。还构建了OYEs超家族的序列相似性网络，以研究特征性OYEs的范围。

关键点

•构建并注释了OYEs超家族的序列相似性网络。

•比较了不同类别的OYE的结构和活性位点。

• “左/右”绑定模式用于解释OYE的立体偏好。

•审查了OYE的结构指导工程，以切换其立体选择性。